NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-85; 263-284 AND 326-345, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
TISSUE=Salivary gland;
DOI=10.1074/jbc.273.46.30583; PubMed=9804829 [NCBI, ExPASy, EBI, Israel, Japan]
Valenzuela J.G., Charlab R., Galperin M.Y., Ribeiro J.M.C.;
"Purification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. A new type of nucleotide-binding enzyme.";
J. Biol. Chem. 273:30583-30590(1998).

Comments

FUNCTION: Inhibits platlet aggregation by the calcium-dependent hydrolysis of ATP and ADP.
CATALYTIC ACTIVITY: ATP + 2 H₂O = AMP + 2 phosphate.
COFACTOR: Calcium.
SIMILARITY: Belongs to the apyrase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF085499; AAD09177.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O96559.

Ontologies

GO:0005615;	Cellular component: extracellular space (non-traceable author statement from UniProtKB).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0030899;	Molecular function: calcium-dependent ATPase activity (inferred from direct assay from UniProtKB).
GO:0017110;	Molecular function: nucleoside-diphosphatase activity (inferred from direct assay from UniProtKB).
GO:0030195;	Biological process: negative regulation of blood coagulation (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR009283; Apyrase.
Graphical view of domain structure.

PANTHER

PTHR13023; Apyrase; 1.

Pfam

PF06079; Apyrase; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

O96559.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; Hydrolase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 35`	`35`
`CHAIN`	`36 364`	`329`	`Apyrase.`	`PRO_0000234527`
`COMPBIAS`	`21 28`	`8`	`Poly-Leu.`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 41474 Da [This is the MW of the unprocessed precursor]

CRC64: C398CB6D29A882DE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSSYRVGNP IRFQPTNVVG LLLLSLVLSF MLVQSYELGH ASGETNANSK YPLTTPVEEN 

        70         80         90        100        110        120 
LKVRFKIGVI SDDDKNAVSK DESNTWVSTY LTGTLEWEKS TDKITVQWDK GNEKKVKSKY 

       130        140        150        160        170        180 
SYGGRGMELS ELVTFNGNLL TFDDRTGLVY ILKDDKVYPW VVLADGDGKN SKGFKSEWAT 

       190        200        210        220        230        240 
EKAGNLYVGS SGKEWTTKEG TIENYNPMWV KMINKNGEVT SLNWQTNYEK IRSSMNITFP 

       250        260        270        280        290        300 
GYMWHEAACW SDKYNKWFFL PRALSQEAYD SKKFETQGAN VIISCDDKFE KCEPTQIQGK 

       310        320        330        340        350        360 
TEDKRGFSNF KFVPTSEDKI IVGLKTVEAD DTTETYFTAF DLEGKVLLEE TKIDDHKYEG 


VDFV

O96559 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools